6JPU

CryoEM structure of Abo1 hexamer - apo complex

6JPU の概要

• エントリーDOI: 10.2210/pdb6jpu/pdb
• 関連するPDBエントリー: 6JPQ
• EMDBエントリー: 9870 9871
• 分子名称: Uncharacterized AAA domain-containing protein C31G5.19 (1 entity in total)
• 機能のキーワード: aaa+ atpase histone chaperone, chaperone
• 由来する生物種: Schizosaccharomyces pombe 972h- (Fission yeast)
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 817364.63

構造登録者

Cho, C.,Jang, J.,Song, J.J. (登録日: 2019-03-28, 公開日: 2019-12-25, 最終更新日: 2024-03-27)

主引用文献

Cho, C.,Jang, J.,Kang, Y.,Watanabe, H.,Uchihashi, T.,Kim, S.J.,Kato, K.,Lee, J.Y.,Song, J.J.
Structural basis of nucleosome assembly by the Abo1 AAA+ ATPase histone chaperone.
Nat Commun, 10:5764-5764, 2019

PubMed Abstract: The fundamental unit of chromatin, the nucleosome, is an intricate structure that requires histone chaperones for assembly. ATAD2 AAA+ ATPases are a family of histone chaperones that regulate nucleosome density and chromatin dynamics. Here, we demonstrate that the fission yeast ATAD2 homolog, Abo1, deposits histone H3-H4 onto DNA in an ATP-hydrolysis-dependent manner by in vitro reconstitution and single-tethered DNA curtain assays. We present cryo-EM structures of an ATAD2 family ATPase to atomic resolution in three different nucleotide states, revealing unique structural features required for histone loading on DNA, and directly visualize the transitions of Abo1 from an asymmetric spiral (ATP-state) to a symmetric ring (ADP- and apo-states) using high-speed atomic force microscopy (HS-AFM). Furthermore, we find that the acidic pore of ATP-Abo1 binds a peptide substrate which is suggestive of a histone tail. Based on these results, we propose a model whereby Abo1 facilitates H3-H4 loading by utilizing ATP.

PubMed: 31848341
DOI: 10.1038/s41467-019-13743-9

実験手法

ELECTRON MICROSCOPY (4.27 Å)